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Bioactive Peptides from Marine By-Products and Underused Marine Organisms

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A special issue of Marine Drugs (ISSN 1660-3397).

Deadline for manuscript submissions: closed (30 July 2021) | Viewed by 28276

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Special Issue Editors

Prof. Dr. Hideki Kishimura

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Guest Editor

Faculty of Fisheries Sciences, Hokkaido University Hakodate, Hokkaido, Japan
Interests: red algae; marine invertebrates; phycoerythrin; xyloorigosaccharide; marine enzymes; marine collagen; chloroplast DNA; antihypertension; prebiotics; antioxidation; antidiabetes
Special Issues, Collections and Topics in MDPI journals

Dr. Yuya Kumagai

E-Mail Website
Guest Editor

Faculty of Fisheries Sciences, Hokkaido University, Hakodate, Hokkaido 041-8611, Japan
Interests: enzymatic character of marine organisms and microorganisms; exploitation of utilization of marine algae; development of genome editing method for marine algae
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

According to “The State of World Fisheries and Aquaculture 2018” published by Food and Agriculture Organization of the United Nations (FAO), fish accounted for about 17% of animal protein consumed by the global population in 2015. By contrast, it is estimated that byproducts occupy about 25 to 35 percent of the total volume of fishmeal and fish oil.

However, fishery byproducts (trimmings, skin, fins, bone, scale, etc.) and underused marine organisms (invertebrates, macro algae, fisheries bycatch, etc.) usually contain a considerable amount of proteins. Therefore, these materials can be considered a potential source of bioactive peptides, as well as nutrition.

This Special Issue aims to accumulate the knowledge of preparation, function, structure, and application of bioactive peptides from fishery byproducts and underused marine organisms. This Special Issue aims to contribute to the achievement of multiple goals of SDGs (No. 2, 3, 12, 14), and we would like to invite scientists to submit their latest research findings in this field. Comprehensive review papers are also welcome.

Prof. Dr. Hideki Kishimura
Dr. Yuya Kumagai
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Marine Drugs is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2900 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

marine by-products
underused marine organisms
protease inhibition
antimicrobial
antioxidant
neuroactive
preparation
structure
application
in silico analysis

Published Papers (9 papers)

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Research

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11 pages, 1771 KiB

Open AccessArticle

Evaluation of the Preservation and Digestion of Seal Meat Processed with Heating and Antioxidant Seal Meat Hydrolysates

by Yi Zhang, Lea Spitzer, Xin Rui, Susana C. M. Fernandes, Romy Vaugeois and Benjamin K. Simpson

Mar. Drugs 2022, 20(3), 204; https://0-doi-org.brum.beds.ac.uk/10.3390/md20030204 - 10 Mar 2022

Viewed by 2844

Abstract

Seal meat is of high nutritive value but is not highly exploited for human food due to ethical issues, undesirable flavors, and loss of nutrients during the processing/cooking step. In this work, commercially available processed seal meat was treated with its hydrolysates as preservatives with the aim of improving nutrient bioavailability. The contents of the nutrients were analyzed after digestion using a simulated dynamic digestion model, and the effects of different processing conditions, i.e., low-temperature processing and storage (25 °C) and high-temperature cooking (100 °C), of seal meat were investigated. Hydrolysates with antioxidant activity decreased the amounts of the less desirable Fe³⁺ ions in the seal meat digests. After treatment with hydrolysates at room temperature, a much higher total Fe content of 781.99 mg/kg was observed compared to other treatment conditions. The release of amino acids increased with temperature and was 520.54 mg/g for the hydrolysate-treated sample versus 413.12 mg/g for the control seal meat sample treated in buffer. Overall, this study provides useful data on the potential use of seal meat as a food product with high nutritive value and seal meat hydrolysates with antioxidant activity as preservatives to control oxidation in food. Full article

(This article belongs to the Special Issue Bioactive Peptides from Marine By-Products and Underused Marine Organisms)

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15 pages, 1848 KiB

Open AccessArticle

Study on the Mechanism of the Blood-Glucose-Lowering Effect of Collagen Peptides from Sturgeon By-Products

by Yukiho Sasaoka, Taichi Takagi, Shunta Michiba, Yohei Yamamoto, Yuya Kumagai and Hideki Kishimura

Mar. Drugs 2021, 19(10), 584; https://0-doi-org.brum.beds.ac.uk/10.3390/md19100584 - 19 Oct 2021

Cited by 4 | Viewed by 2426

Abstract

In a previous study, we found that the collagen peptides prepared from the by-products of Bester sturgeon had an inhibitory effect on elevated blood glucose levels in a glucose tolerance test with ICR mice. In the present study, we examine the mechanism of the effect of sturgeon collagen peptides (SCPs) in detail. When glucose was orally administered to mice along with the SCPs, it was found that the glucose remained in the stomach for a longer time. In the above tests, the amount of glucose excreted in the feces of mice also increased. On the contrary, it was revealed that the SCPs have a dipeptidyl-peptidase-IV (DPP-IV) inhibitory ability in an in vitro test. In subsequent oral and intravenous glucose administration tests, glucagon-like peptide-1 (GLP-1) and insulin levels in the blood of mice were maintained at high levels. These results suggested the following three mechanisms: SCPs slow the rate of transportation of glucose from the stomach into the small intestine, resulting in delayed glucose absorption; SCPs suppress the absorption of glucose in the small intestine and excrete it from the body; SCPs inhibit DPP-IV in the blood and maintain a high GLP-1 level in blood, which in turn stimulates insulin secretion. Full article

(This article belongs to the Special Issue Bioactive Peptides from Marine By-Products and Underused Marine Organisms)

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15 pages, 3022 KiB

Open AccessArticle

Identifying Potential Antioxidant Properties from the Viscera of Sea Snails (Turbo cornutus)

by Nalae Kang, Eun-A Kim, Junseong Kim, Seung-Hong Lee and Soo-Jin Heo

Mar. Drugs 2021, 19(10), 567; https://0-doi-org.brum.beds.ac.uk/10.3390/md19100567 - 13 Oct 2021

Cited by 13 | Viewed by 2530

Abstract

Turbo cornutus, the horned turban sea snail, is found along the intertidal and basaltic shorelines of Jeju Island, Korea. T. cornutus feeds on seaweeds (e.g., Undaria sp., and Ecklonia sp.) composed of diverse antioxidants. This study identified potential antioxidant properties from T. cornutus viscera tissues. Diverse extracts were evaluated for their hydrogen peroxide (H₂O₂) scavenging activities. T. cornutus viscera protamex-assisted extracts (TVP) were purified by gel filtration chromatography (GFC), and potential antioxidant properties were analyzed for their amino acid sequences and its peroxidase inhibition effects by in silico molecular docking and in vitro analysis. According to the results, T. cornutus viscera tissues are composed of many protein contents with each over 50%. Among the extracts, TVP possessed the highest H₂O₂ scavenging activity. In addition, TVP-GFC-3 significantly decreased intracellular reactive oxygen species (ROS) levels and increased cell viability in H₂O₂-treated HepG2 cells without cytotoxicity. TVP-GFC-3 comprises nine low molecular bioactive peptides (ELR, VGPQ, TDY, ALPHA, PAH, VDY, WSDK, VFSP, and FAPQY). Notably, the peptides dock to the active site of the myeloperoxidase (MPO), especially TDY and FAPQY showed the MPO inhibition effects with IC₅₀ values of 646.0 ± 45.0 µM and 57.1 ± 17.7 µM, respectively. Altogether, our findings demonstrated that T. cornutus viscera have potential antioxidant properties that can be used as high value-added ingredients. Full article

(This article belongs to the Special Issue Bioactive Peptides from Marine By-Products and Underused Marine Organisms)

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14 pages, 9141 KiB

Open AccessArticle

Purification and Identification of Novel Xanthine Oxidase Inhibitory Peptides Derived from Round Scad (Decapterus maruadsi) Protein Hydrolysates

by Xiao Hu, Ya Zhou, Shaobo Zhou, Shengjun Chen, Yanyan Wu, Laihao Li and Xianqing Yang

Mar. Drugs 2021, 19(10), 538; https://0-doi-org.brum.beds.ac.uk/10.3390/md19100538 - 24 Sep 2021

Cited by 11 | Viewed by 2481

Abstract

The objective of the present study was to investigate the xanthine oxidase (XO) inhibitory effects of peptides purified and identified from round scad (Decapterus maruadsi) hydrolysates (RSHs). In this study, RSHs were obtained by using three proteases (neutrase, protamex and alcalase). Among them, the RSHs of 6-h hydrolysis by neutrase displayed the strongest XO inhibitory activity and had an abundance of small peptides (<500 Da). Four novel peptides were purified by immobilized metal affinity chromatography and identified by nano-high-performance liquid chromatography mass/mass spectrometry. Their amino acid sequences were KGFP (447.53 Da), FPSV (448.51 Da), FPFP (506.59 Da) and WPDGR (629.66 Da), respectively. Then the peptides were synthesized to evaluate their XO inhibitory activity. The results indicated that the peptides of both FPSV (5 mM) and FPFP (5 mM) exhibited higher XO inhibitory activity (22.61 ± 1.81% and 20.09 ± 2.41% respectively). Fluorescence spectra assay demonstrated that the fluorescence quenching mechanism of XO by these inhibitors (FPSV and FPFP) was a static quenching procedure. The study of inhibition kinetics suggested that the inhibition of both FPSV and FPFP was reversible, and the type of their inhibition was a mixed one. Molecular docking revealed the importance of π-π stacking between Phe residue (contained in peptides) and Phe⁹¹⁴ (contained in the XO) in the XO inhibitory activity of the peptides. Full article

(This article belongs to the Special Issue Bioactive Peptides from Marine By-Products and Underused Marine Organisms)

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16 pages, 2963 KiB

Open AccessArticle

Antimicrobial Activity and Action Mechanisms of Arg-Rich Short Analog Peptides Designed from the C-Terminal Loop Region of American Oyster Defensin (AOD)

by Jung-Kil Seo, Dong-Gyun Kim, Ji-Eun Lee, Kwon-Sam Park, In-Ah Lee, Ki-Young Lee, Young-Ok Kim and Bo-Hye Nam

Mar. Drugs 2021, 19(8), 451; https://0-doi-org.brum.beds.ac.uk/10.3390/md19080451 - 06 Aug 2021

Cited by 9 | Viewed by 2374

Abstract

American oyster defensin (AOD) was previously purified from acidified gill extract of the American oyster, Crassostrea virginica. AOD is composed of 38 amino acids with three disulfide bonds and exhibits strong antimicrobial activity against Gram-positive bacteria as well as significant activity against Gram-negative bacteria. Here, to develop promising peptides into antibiotic candidates, we designed five arginine-rich analogs (A0, A1, A2, A3, and A4), predicted their loop and extended strand/random structures—including nine amino acids and a disulfide bond derived from the C-terminus of AOD—and described their antimicrobial and cytotoxic effects, as well as their modes of action. In our experimental results, the A3 and A4 analogs exhibited potent antimicrobial activity against all test organisms—including four Gram-positive bacteria, six Gram-negative bacteria, and Candida albicans—without cell toxicity. A sequence of experiments, including a membrane permeabilization assay, DNA binding study, and DNA polymerization inhibition test, indicated that the two analogs (A3 and A4) possibly did not act directly on the bacterial membrane but instead interacted with intracellular components such as DNA or DNA amplification reactions. AOD analogs also showed strong bacterial inhibition activity in the plasma environment. In addition, analog-treated microbial cells clearly exhibited membrane disruption, damage, and leakage of cytoplasmic contents. Collectively, our results suggest that two analogs, A3 and A4, have potent antimicrobial activity via DNA interaction and have the potential for development into novel antimicrobial agents. Full article

(This article belongs to the Special Issue Bioactive Peptides from Marine By-Products and Underused Marine Organisms)

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13 pages, 2868 KiB

Open AccessArticle

Characterization of ACE Inhibitory Peptides Prepared from Pyropia pseudolinearis Protein

by Yuya Kumagai, Keigo Toji, Satoshi Katsukura, Rie Morikawa, Toshiki Uji, Hajime Yasui, Takeshi Shimizu and Hideki Kishimura

Mar. Drugs 2021, 19(4), 200; https://0-doi-org.brum.beds.ac.uk/10.3390/md19040200 - 01 Apr 2021

Cited by 19 | Viewed by 3541

Abstract

More than 7000 red algae species have been classified. Although most of them are underused, they are a protein-rich marine resource. The hydrolysates of red algal proteins are good candidates for the inhibition of the angiotensin-I-converting enzyme (ACE). The ACE is one of the key factors for cardiovascular disease, and the inhibition of ACE activity is related to the prevention of high blood pressure. To better understand the relationship between the hydrolysates of red algal proteins and the inhibition of ACE activity, we attempted to identify novel ACE inhibitory peptides from Pyropia pseudolinearis. We prepared water soluble proteins (WSP) containing phycoerythrin, phycocyanin, allophycocyanin, and ribulose 1,5-bisphosphate carboxylase/oxygenase. In vitro analysis showed that the thermolysin hydrolysate of the WSP had high ACE inhibitory activity compared to that of WSP. We then identified 42 peptides in the hydrolysate by high-performance liquid chromatography and mass spectrometry. Among 42 peptides, 23 peptides were found in chloroplast proteins. We then synthesized the uncharacterized peptides ARY, YLR, and LRM and measured the ACE inhibitory activity. LRM showed a low IC₅₀ value (0.15 μmol) compared to ARY and YLR (1.3 and 5.8 μmol). In silico analysis revealed that the LRM sequence was conserved in cpcA from Bangiales and Florideophyceae, indicating that the novel ACE inhibitory peptide LRM was highly conserved in red algae. Full article

(This article belongs to the Special Issue Bioactive Peptides from Marine By-Products and Underused Marine Organisms)

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14 pages, 2517 KiB

Open AccessArticle

Amino Acid Profiles and Biopotentiality of Hydrolysates Obtained from Comb Penshell (Atrina pectinata) Viscera Using Subcritical Water Hydrolysis

by Hee-Jeong Lee, Vikash Chandra Roy, Truc Cong Ho, Jin-Seok Park, Yu-Rin Jeong, Seung-Chan Lee, Sung-Yeol Kim and Byung-Soo Chun

Mar. Drugs 2021, 19(3), 137; https://0-doi-org.brum.beds.ac.uk/10.3390/md19030137 - 01 Mar 2021

Cited by 22 | Viewed by 3249

Abstract

The recovery of amino acids and other important bioactive compounds from the comb penshell (Atrina pectinata) using subcritical water hydrolysis was performed. A wide range of extraction temperatures from 140 to 290 °C was used to evaluate the release of proteins and amino acids. The amount of crude protein was the highest (36.14 ± 1.39 mg bovine serum albumin/g) at 200 °C, whereas a further increase in temperature showed the degradation of the crude protein content. The highest amount of amino acids (74.80 mg/g) was at 230 °C, indicating that the temperature range of 170–230 °C is suitable for the extraction of protein-rich compounds using subcritical water hydrolysis. Molecular weights of the peptides obtained from comb penshell viscera decreased with the increasing temperature. SDS-PAGE revealed that the molecular weight of peptides present in the hydrolysates above the 200 °C extraction temperature was ≤ 1000 Da. Radical scavenging activities were analyzed to evaluate the antioxidant activities of the hydrolysates. A. pectinata hydrolysates also showed a particularly good antihypertensive activity, proving that this raw material can be an effective source of amino acids and marine bioactive peptides. Full article

(This article belongs to the Special Issue Bioactive Peptides from Marine By-Products and Underused Marine Organisms)

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Review

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19 pages, 677 KiB

Open AccessReview

Antiaging Potential of Peptides from Underused Marine Bioresources

by Enqin Xia, Xuan Zhu, Xuebin Gao, Jindong Ni and Honghui Guo

Mar. Drugs 2021, 19(9), 513; https://0-doi-org.brum.beds.ac.uk/10.3390/md19090513 - 10 Sep 2021

Cited by 5 | Viewed by 3109

Abstract

Aging is a biological process that occurs under normal conditions and in several chronic degenerative diseases. Bioactive natural peptides have been shown to improve the effects of aging in cell and animal models and in clinical trials. However, few reports delve into the enormous diversity of peptides from marine organisms. This review provides recent information on the antiaging potential of bioactive peptides from underused marine resources, including examples that scavenge free radicals in vitro, inhibit cell apoptosis, prolong the lifespan of fruit flies and Caenorhabditis elegans, suppress aging in mice, and exert protective roles in aging humans. The underlying molecular mechanisms involved, such as upregulation of oxidase activity, inhibition of cell apoptosis and MMP-1 expression, restoring mitochondrial function, and regulating intestinal homeostasis, are also summarized. This work will help highlight the antiaging potential of peptides from underused marine organisms which could be used as antiaging foods and cosmetic ingredients in the near future. Full article

(This article belongs to the Special Issue Bioactive Peptides from Marine By-Products and Underused Marine Organisms)

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22 pages, 7324 KiB

Open AccessReview

Exploiting of Secondary Raw Materials from Fish Processing Industry as a Source of Bioactive Peptide-Rich Protein Hydrolysates

by Girija Gajanan Phadke, Nikheel Bhojraj Rathod, Fatih Ozogul, Krishnamoorthy Elavarasan, Muthusamy Karthikeyan, Kyung-Hoon Shin and Se-Kwon Kim

Mar. Drugs 2021, 19(9), 480; https://0-doi-org.brum.beds.ac.uk/10.3390/md19090480 - 25 Aug 2021

Cited by 20 | Viewed by 4288

Abstract

Developing peptide-based drugs are very promising to address many of the lifestyle mediated diseases which are prevalent in a major portion of the global population. As an alternative to synthetic peptide-based drugs, derived peptides from natural sources have gained a greater attention in the last two decades. Aquatic organisms including plants, fish and shellfish are known as a rich reservoir of parent protein molecules which can offer novel sequences of amino acids in peptides, having unique bio-functional properties upon hydrolyzing with proteases from different sources. However, rather than exploiting fish and shellfish stocks which are already under pressure due to overexploitation, the processing discards, regarded as secondary raw material, could be a potential choice for peptide based therapeutic development strategies. In this connection, we have attempted to review the scientific reports in this area of research that deal with some of the well-established bioactive properties, such as antihypertensive, anti-oxidative, anti-coagulative, antibacterial and anticarcinogenic properties, with reference to the type of enzymes, substrate used, degree of particular bio-functionality, mechanism, and wherever possible, the active amino acid sequences in peptides. Many of the studies have been conducted on hydrolysate (crude mixture of peptides) enriched with low molecular bioactive peptides. In vitro and in vivo experiments on the potency of bioactive peptides to modulate the human physiological functions beneficially have demonstrated that these peptides can be used in the prevention and treatment of non-communicable lifestyle mediated diseases. The information synthesized under this review could serve as a point of reference to drive further research on and development of functionally active therapeutic natural peptides. Availability of such scientific information is expected to open up new zones of investigation for adding value to underutilized secondary raw materials, which in turn paves the way for sustainability in fish processing. However, there are significant challenges ahead in exploring the fish waste as a source of bioactive peptides, as it demands more studies on mechanisms and structure–function relationship understanding as well as clearance from regulatory and statutory bodies before reaching the end user in the form of supplement or therapeutics. Full article

(This article belongs to the Special Issue Bioactive Peptides from Marine By-Products and Underused Marine Organisms)

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